Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO

Michael Chapman, Se Won Suh, Duilio Cascio, Ward W. Smith, David Eisenberg

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 Å along the 4-fold axis and 132 Å in diameter at the widest point of the keg3-6. Here we describe the quaternary structure of RuBisCO from N. tabacum, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution (3 Å). The structure shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy5,6. The structure, with its elongated and inter-digitated L subunits, is evidence against a large, sliding-layer conformational change in plant RuBisCO, as proposed recently in Nature for the same enzyme from Alcaligenes eutrophus7.

Original languageEnglish (US)
Pages (from-to)354-356
Number of pages3
JournalNature
Volume329
Issue number6137
StatePublished - 1987
Externally publishedYes

Fingerprint

Plant Structures
Alcaligenes
Oxygenases
Photosynthesis
Enzymes
Carbon Dioxide
Catalytic Domain
X-Rays
Electrons
Bacteria
ribulose

ASJC Scopus subject areas

  • General

Cite this

Chapman, M., Suh, S. W., Cascio, D., Smith, W. W., & Eisenberg, D. (1987). Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO. Nature, 329(6137), 354-356.

Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO. / Chapman, Michael; Suh, Se Won; Cascio, Duilio; Smith, Ward W.; Eisenberg, David.

In: Nature, Vol. 329, No. 6137, 1987, p. 354-356.

Research output: Contribution to journalArticle

Chapman, M, Suh, SW, Cascio, D, Smith, WW & Eisenberg, D 1987, 'Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO', Nature, vol. 329, no. 6137, pp. 354-356.
Chapman M, Suh SW, Cascio D, Smith WW, Eisenberg D. Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO. Nature. 1987;329(6137):354-356.
Chapman, Michael ; Suh, Se Won ; Cascio, Duilio ; Smith, Ward W. ; Eisenberg, David. / Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO. In: Nature. 1987 ; Vol. 329, No. 6137. pp. 354-356.
@article{1f254ef05ff343e8b3a2c76c504c4655,
title = "Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO",
abstract = "RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 {\AA} along the 4-fold axis and 132 {\AA} in diameter at the widest point of the keg3-6. Here we describe the quaternary structure of RuBisCO from N. tabacum, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution (3 {\AA}). The structure shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy5,6. The structure, with its elongated and inter-digitated L subunits, is evidence against a large, sliding-layer conformational change in plant RuBisCO, as proposed recently in Nature for the same enzyme from Alcaligenes eutrophus7.",
author = "Michael Chapman and Suh, {Se Won} and Duilio Cascio and Smith, {Ward W.} and David Eisenberg",
year = "1987",
language = "English (US)",
volume = "329",
pages = "354--356",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6137",

}

TY - JOUR

T1 - Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO

AU - Chapman, Michael

AU - Suh, Se Won

AU - Cascio, Duilio

AU - Smith, Ward W.

AU - Eisenberg, David

PY - 1987

Y1 - 1987

N2 - RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 Å along the 4-fold axis and 132 Å in diameter at the widest point of the keg3-6. Here we describe the quaternary structure of RuBisCO from N. tabacum, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution (3 Å). The structure shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy5,6. The structure, with its elongated and inter-digitated L subunits, is evidence against a large, sliding-layer conformational change in plant RuBisCO, as proposed recently in Nature for the same enzyme from Alcaligenes eutrophus7.

AB - RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 Å along the 4-fold axis and 132 Å in diameter at the widest point of the keg3-6. Here we describe the quaternary structure of RuBisCO from N. tabacum, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution (3 Å). The structure shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy5,6. The structure, with its elongated and inter-digitated L subunits, is evidence against a large, sliding-layer conformational change in plant RuBisCO, as proposed recently in Nature for the same enzyme from Alcaligenes eutrophus7.

UR - http://www.scopus.com/inward/record.url?scp=0023663713&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023663713&partnerID=8YFLogxK

M3 - Article

VL - 329

SP - 354

EP - 356

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6137

ER -